Rikihisa Y
Anat Rec. 1985 Jan;211(1):1-8. doi: 10.1002/ar.1092110102.
Ultrastructural localization of carbonic anhydrase was determined by applying Hansson's histochemical method to glutaraldehyde-fixed frozen sections of guinea pig peritoneal polymorphonuclear leukocytes (PMNs) and lysosomes isolated from rat liver tissue after the animal had been injected with Triton WR-1339. A positive histochemical reaction for carbonic anhydrase in PMNs was found in the matrix of lysosomes. After PMNs phagocytized polystyrene latex particles or emulsified paraffin oil droplets, a positive reactivity for carbonic anhydrase was found in the space between the lysosomal membrane and the particle. Liver lysosomes also revealed positive carbonic anhydrase histochemical reactivity. To confirm the histochemical reaction, indirect immunoferritin labeling was conducted with rabbit antibody to human red blood cell carbonic anhydrase C on glutaraldehyde-fixed, freeze-thawed human PMNs. Immunolabeling was observed in lysosomes. These results suggest that carbonic anhydrase is a constituent of lysosomes of PMNs and liver cells.
通过将汉森组织化学方法应用于豚鼠腹膜多形核白细胞（PMN）的戊二醛固定冰冻切片以及给动物注射曲拉通WR - 1339后从大鼠肝脏组织分离的溶酶体，来确定碳酸酐酶的超微结构定位。在PMN的溶酶体基质中发现了碳酸酐酶的阳性组织化学反应。PMN吞噬聚苯乙烯乳胶颗粒或乳化石蜡油滴后，在溶酶体膜与颗粒之间的空间发现了碳酸酐酶的阳性反应性。肝溶酶体也显示出碳酸酐酶组织化学阳性反应性。为了证实组织化学反应，用抗人红细胞碳酸酐酶C的兔抗体对戊二醛固定、冻融的人PMN进行间接免疫铁蛋白标记。在溶酶体中观察到免疫标记。这些结果表明碳酸酐酶是PMN和肝细胞溶酶体的一个组成部分。
